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dc.contributor.authorHan, Qianen_US
dc.contributor.authorDing, Haizhenen_US
dc.contributor.authorRobinson, Howarden_US
dc.contributor.authorChristensen, Bruce M.en_US
dc.contributor.authorLi, Jianyongen_US
dc.date.accessioned2018-11-13T14:06:48Z
dc.date.available2018-11-13T14:06:48Z
dc.date.issued2010-01-21en_US
dc.identifier.othere8826en_US
dc.identifier.urihttp://hdl.handle.net/10919/85827
dc.description.abstractBackground 3,4-Dihydroxyphenylalanine decarboxylase (DDC), also known as aromatic L-amino acid decarboxylase, catalyzes the decarboxylation of a number of aromatic L-amino acids. Physiologically, DDC is responsible for the production of dopamine and serotonin through the decarboxylation of 3,4-dihydroxyphenylalanine and 5-hydroxytryptophan, respectively. In insects, both dopamine and serotonin serve as classical neurotransmitters, neuromodulators, or neurohormones, and dopamine is also involved in insect cuticle formation, eggshell hardening, and immune responses. Principal Findings In this study, we expressed a typical DDC enzyme from Drosophila melanogaster, critically analyzed its substrate specificity and biochemical properties, determined its crystal structure at 1.75 Angstrom resolution, and evaluated the roles residues T82 and H192 play in substrate binding and enzyme catalysis through site-directed mutagenesis of the enzyme. Our results establish that this DDC functions exclusively on the production of dopamine and serotonin, with no activity to tyrosine or tryptophan and catalyzes the formation of serotonin more efficiently than dopamine. Conclusions The crystal structure of Drosophila DDC and the site-directed mutagenesis study of the enzyme demonstrate that T82 is involved in substrate binding and that H192 is used not only for substrate interaction, but for cofactor binding of drDDC as well. Through comparative analysis, the results also provide insight into the structure-function relationship of other insect DDC-like proteins.en_US
dc.format.mimetypeapplication/pdfen_US
dc.language.isoen_USen_US
dc.publisherPLOSen_US
dc.rightsCreative Commons Attribution 4.0 Internationalen_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.titleCrystal Structure and Substrate Specificity of Drosophila 3,4-Dihydroxyphenylalanine Decarboxylaseen_US
dc.typeArticle - Refereeden_US
dc.description.versionPeer Revieweden_US
dc.contributor.departmentBiochemistryen_US
dc.title.serialPLOS ONEen_US
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0008826en_US
dc.identifier.volume5en_US
dc.identifier.issue1en_US
dc.type.dcmitypeTexten_US
dc.identifier.pmid20098687en_US
dc.identifier.eissn1932-6203en_US


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Creative Commons Attribution 4.0 International
License: Creative Commons Attribution 4.0 International